Recombinant Phospho-Jun, JunD (Ser73, Ser100) Monoclonal Antibody (AN301147L)
For research use only.
| Verified Samples | Verified Samples in WB: Hela |
| Dilution | WB 1:2000-1:10000 |
| Isotype | IgG,κ |
| Host | Rabbit |
| Reactivity | Human, Mouse, Rat |
| Applications | WB |
| Clonality | Monoclonal;Recombinant |
| Immunogen | A synthetic peptide corresponding to residues around (Ser73, Ser100) of Human Phospho-Jun, JunD |
| Abbre | Jun, JunD |
| Synonyms | AP-1, AP1, c-Jun, JUN, c, Activator protein 1, AP 1, AP-1 transcription factor subunit, cJun, Enhancer Binding Protein AP1, Jun Activation Domain Binding Protein, Jun oncogene, JUN protein, Jun proto oncogene, Jun proto-oncogene, JUNC, Oncogene JUN, p39, Proto oncogene c jun, Proto oncogene cJun, Proto-oncogene c-jun, Transcription Factor AP 1, Transcription Factor AP1, Transcription factor AP-1, V jun avian sarcoma virus 17 oncogene homolog, V jun sarcoma virus 17 oncogene homolog, V jun sarcoma virus 17 oncogene homolog (avian), vJun Avian Sarcoma Virus 17 Oncogene Homolog, V-jun avian sarcoma virus 17 oncogene homolog, c-JUN |
| Swissprot | |
| Calculated MW | 35 kDa,36 kDa |
| Observed MW |
42 kDa,48 kDa
The actual band is not consistent with the expectation.
Western blotting is a method for detecting a certain protein in a complex sample based on the specific binding of antigen and antibody. Different proteins can be divided into bands based on different mobility rates. The mobility is affected by many factors, which may cause the observed band size to be inconsistent with the expected size. The common factors include: 1. Post-translational modifications: For example, modifications such as glycosylation, phosphorylation, methylation, and acetylation will increase the molecular weight of the protein. 2. Splicing variants: Different expression patterns of various mRNA splicing bodies may produce proteins of different sizes. 3. Post-translational cleavage: Many proteins are first synthesized into precursor proteins and then cleaved to form active forms, such as COL1A1. 4. Relative charge: the composition of amino acids (the proportion of charged amino acids and uncharged amino acids). 5. Formation of multimers: For example, in protein dimer, strong interactions between proteins can cause the bands to be larger. However, the use of reducing conditions can usually avoid the formation of multimers. If a protein in a sample has different modified forms at the same time, multiple bands may be detected on the membrane. |
| Cellular Localization | Nucleus |
| Concentration | 0.2 mg/mL |
| Buffer | PBS, 50% glycerol, 0.05% Proclin 300, 0.05% protein protectant. |
| Purification Method | Protein A |
| Research Areas | Epigenetics and Nuclear Signaling, Signal Transduction, Cancer, Immunology, Kits, Lysates, Other, Cardiovascular |
| Clone No. | 6H8 |
| Conjugation | Unconjugated |
| Storage | Store at -20°C Valid for 12 months. Avoid freeze / thaw cycles. |
| Shipping | Ice bag |
| background | This gene is the putative transforming gene of avian sarcoma virus 17. It encodes a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. This gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies. |
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Unconjugated
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